1MUH

CRYSTAL STRUCTURE OF TN5 TRANSPOSASE COMPLEXED WITH TRANSPOSON END DNA

Replaces:  1F3I

Summary for 1MUH

• Entry DOI: 10.2210/pdb1muh/pdb
• Descriptor: DNA TRANSFERRED STRAND, DNA NON-TRANSFERRED STRAND, Tn5 transposase, ... (6 entities in total)
• Functional Keywords: transposase, ribonuclease h-like motif, protein-dna complex, synaptic complex, transcription-dna complex, transcription/dna
• Biological source: Escherichia coli; More
• Total number of polymer chains: 3
• Total formula weight: 66190.88

Authors

Thoden, J.B.,Holden, H.M.,Davies, D.R.,Goryshin, I.Y.,Reznikoff, W.S.,Rayment, I. (deposition date: 2002-09-23, release date: 2002-09-27, Last modification date: 2024-02-14)

Primary citation

Davies, D.R.,Goryshin, I.Y.,Reznikoff, W.S.,Rayment, I.
Three-dimensional structure of the Tn5 synaptic complex transposition intermediate.
Science, 289:77-85, 2000

PubMed Abstract: Genomic evolution has been profoundly influenced by DNA transposition, a process whereby defined DNA segments move freely about the genome. Transposition is mediated by transposases, and similar events are catalyzed by retroviral integrases such as human immunodeficiency virus-1 (HIV-1) integrase. Understanding how these proteins interact with DNA is central to understanding the molecular basis of transposition. We report the three-dimensional structure of prokaryotic Tn5 transposase complexed with Tn5 transposon end DNA determined to 2.3 angstrom resolution. The molecular assembly is dimeric, where each double-stranded DNA molecule is bound by both protein subunits, orienting the transposon ends into the active sites. This structure provides a molecular framework for understanding many aspects of transposition, including the binding of transposon end DNA by one subunit and cleavage by a second, cleavage of two strands of DNA by a single active site via a hairpin intermediate, and strand transfer into target DNA.

PubMed: 10884228
DOI: 10.1126/science.289.5476.77

Experimental method

X-RAY DIFFRACTION (2.3 Å)